ID A0A2S5B4Y3_9BASI Unreviewed; 473 AA.
AC A0A2S5B4Y3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03125};
DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125};
DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125};
GN ORFNames=BMF94_5201 {ECO:0000313|EMBL:POY71840.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY71840.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY71840.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY71840.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC commited step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-
CC Rule:MF_03125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POY71840.1}.
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DR EMBL; PJQD01000072; POY71840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B4Y3; -.
DR STRING; 741276.A0A2S5B4Y3; -.
DR OrthoDB; 122722at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03125}; Reference proteome {ECO:0000313|Proteomes:UP000237144}.
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 85..88
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 87..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 180
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 194
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 271
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 286
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 346..352
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 350
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 378..380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 461..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
SQ SEQUENCE 473 AA; 51817 MW; 93C9CD0F6DBE6C7C CRC64;
MASTTPPNQV EVVLGAQWGD LFAELNPRRT AELMPKLVFA VVPGKQEGKS NLLSAPHWLS
EGKGKLVDIL AGEVDICARC AGGNNAGHTI VATIDGKKTK FDFHLLPSGL VNPNCTAFIG
NGVVVHIPAF FQELDTLISK GLNCDGRLFV SDRAHLVFDF HQIVDGLKEV ELGGSNIGTT
RKGIGPAYSS KSSRSGLRVH HLFDEEAFAT KFRKLVEGRF KRYGQFEYDT EGEILRYKEL
AKRLKPFVVD GVSFMHDALA QNKRILVEGA NALMLDLDFG TYPFVTSSAT GIGGVCTGLG
LPPKAIGETY GVIKAYTTRV GSGPFPTEQL NKIGEHLQEV GAEFGVTTGR RRRCGWLDLV
VMKYSTLING YTALNLTKLD VLDDLEEIQV ATAYYLDGKP LPALFPADLD VLARVEVKYE
TLPGWKQSIQ DVTKFEDLPK TCQEYVLFIE KFLGVPVKFI GTGPARESMI VKQ
//
